Zinc binding to a conserved motif in STIM1 induces clustering and SOCE activation.

ABSTRACT:

Background

STIM1 is a key regulator of calcium homeostasis in the endoplasmic reticulum (ER), activated upon ER calcium depletion through calcium dissociation from its EF-hand domain. While much is known about its domain organization and activation-induced structural rearrangements, certain regulatory mechanisms remain unclear. A short conserved region upstream of the EF-hand has been previously implicated in redox modulation of STIM1, but its exact function was unknown.

Methods

We used a combination of biochemical assays, mutagenesis, and imaging approaches to investigate the structural and functional role of this conserved region. Zinc binding was assessed by spectroscopy, and STIM1 clustering was monitored by fluorescence microscopy. Statistical analyses were applied wher

SUBMITTER: Alary B 

PROVIDER: S-EPMC12639717 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature